Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress. - Wikidata - awgldk - TriplyDB

Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Differential regulation of TRPV1 channels by H2O2: implications for diabetic microvascular dysfunction.Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion Redox regulation of mitochondrial function High-Protein Intake during Weight Loss Therapy Eliminates the Weight-Loss-Induced Improvement in Insulin Action in Obese Postmenopausal Women Identification of cardiac myosin-binding protein C as a candidate biomarker of myocardial infarction by proteomics analysis Caenorhabditis elegans: A useful model for studying metabolic disorders in which oxidative stress is a contributing factor.Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Nox4 regulates Nrf2 and glutathione redox in cardiomyocytes in vivo.Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities Hydrogen peroxide sensing and signaling by protein kinases in the cardiovascular system.Reactive oxygen species and the cardiovascular system Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation Roles for cytosolic NADPH redox in regulating pulmonary artery relaxation by thiol oxidation-elicited subunit dimerization of protein kinase G1α Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins.Protection of peroxiredoxin II on oxidative stress-induced cardiomyocyte death and apoptosis.Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling.Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation.Hydrogen peroxide modifies human sperm peroxiredoxins in a dose-dependent manner.Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion.THE MULTI-FACETED IMPACT OF PEROXIREDOXINS ON AGING AND DISEASE.Alterations in NO/ROS ratio and expression of Trx1 and Prdx2 in isoproterenol-induced cardiac hypertrophy.Short-term use of telmisartan attenuates oxidation and improves Prdx2 expression more than antioxidant β-blockers in the cardiovascular systems of spontaneously hypertensive rats.Peroxiredoxin as a functional endogenous antioxidant enzyme in pronuclei of mouse zygotes.

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P2860

Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

http://www.wikidata.org/entity/Q36807991

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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AJPHEART.00017.2008

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American Journal of Physiology - Heart and Circulatory Physiology

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Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress.

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P2093

Ewald Schröder

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Jonathan P Brennan

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Philip Eaton

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P2860

Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site

Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation

Crystal structure of a dimeric oxidized form of human peroxiredoxin 5

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C

Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution

ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.

Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function.

Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2

Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression

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10.1152/AJPHEART.00017.2008

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1

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2494773

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